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Table representation of search results timeline featuring number of search results per year.

Year Number of Results
1911 1
1913 1
1916 1
1917 3
1921 2
1922 1
1923 1
1924 1
1926 2
1928 1
1929 1
1933 3
1934 3
1935 2
1936 2
1941 1
1942 1
1943 1
1944 2
1945 20
1946 77
1947 76
1948 55
1949 41
1950 70
1951 91
1952 88
1953 117
1954 144
1955 186
1956 203
1957 236
1958 246
1959 231
1960 201
1961 237
1962 261
1963 408
1964 568
1965 503
1966 514
1967 567
1968 699
1969 772
1970 866
1971 1083
1972 1160
1973 1180
1974 1368
1975 1300
1976 1129
1977 1193
1978 1200
1979 1334
1980 1454
1981 1604
1982 1467
1983 1575
1984 1680
1985 1734
1986 1638
1987 1802
1988 1866
1989 2157
1990 2286
1991 2127
1992 2387
1993 2331
1994 2398
1995 2379
1996 2383
1997 2482
1998 2521
1999 2539
2000 2771
2001 2902
2002 3141
2003 3344
2004 3648
2005 4103
2006 4402
2007 4920
2008 5255
2009 5570
2010 5856
2011 6448
2012 6905
2013 7562
2014 7701
2015 8061
2016 8185
2017 8234
2018 8202
2019 8452
2020 9186
2021 9364
2022 9221
2023 8098
2024 2352

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193,920 results

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Page 1
HUMAN HAEMOGLOBINS.
HUEHNS ER, SHOOTER EM. HUEHNS ER, et al. J Med Genet. 1965 Mar;2(1):48-90. doi: 10.1136/jmg.2.1.48. J Med Genet. 1965. PMID: 14296925 Free PMC article. Review. No abstract available.
Structure and function of haemoglobins.
Gell DA. Gell DA. Blood Cells Mol Dis. 2018 May;70:13-42. doi: 10.1016/j.bcmd.2017.10.006. Epub 2017 Oct 31. Blood Cells Mol Dis. 2018. PMID: 29126700 Review.
Haemoglobin (Hb) is widely known as the iron-containing protein in blood that is essential for O(2) transport in mammals. ...
Haemoglobin (Hb) is widely known as the iron-containing protein in blood that is essential for O(2) transport in mammals. ...
[Hemoglobin, from microorganisms to man: a single structural motif, multiple functions].
Wajcman H, Kiger L. Wajcman H, et al. C R Biol. 2002 Dec;325(12):1159-74. doi: 10.1016/s1631-0691(02)01537-8. C R Biol. 2002. PMID: 12520866 Free article. Review. French.
Elsewhere haemoglobin may act as final electron acceptors in oxido-reduction pathways. Evolution of haemoglobin in invertebrates followed a large variety of scenarios. ...
Elsewhere haemoglobin may act as final electron acceptors in oxido-reduction pathways. Evolution of haemoglobin in invertebrat …
[Expression of recombinant human hemoglobin in plants].
Dieryck W, Gruber V, Baudino S, Lenee P, Pagnier J, Merot B, Poyart C. Dieryck W, et al. Transfus Clin Biol. 1995;2(6):441-7. doi: 10.1016/s1246-7820(05)80069-2. Transfus Clin Biol. 1995. PMID: 8646339 Review. French.
Human utilization of recombinant proteins of therapeutical interest, as hemoglobin, implies that the transgenic host allows a low cost production of the active proteins with minimal risks of pathogen contamination. ...
Human utilization of recombinant proteins of therapeutical interest, as hemoglobin, implies that the transgenic host allows a
Surface activity of hemoglobin S and other human hemoglobin variants.
Elbaum D, Harrington J, Roth EF Jr, Nagel RL. Elbaum D, et al. Biochim Biophys Acta. 1976 Mar 18;427(1):57-69. doi: 10.1016/0005-2795(76)90285-3. Biochim Biophys Acta. 1976. PMID: 1260008
The kinetics of surface pressure change (deltapi vs. t isotherms) were determined for several single point mutations of the human hemoglobin system. It was observed that hemoglobin S and hemoglobin CHarlem (both containing beta6 Glu leads to Val …
The kinetics of surface pressure change (deltapi vs. t isotherms) were determined for several single point mutations of the human
Abnormal human haemoglobins.
INGRAM VM. INGRAM VM. Proc R Soc Med. 1958 Aug;51(8):645-6. Proc R Soc Med. 1958. PMID: 13578968 Free article. No abstract available.
Interaction of human hemoglobin and its variants with agar.
Winter WP, Yodh J. Winter WP, et al. Science. 1983 Jul 8;221(4606):175-8. doi: 10.1126/science.6190229. Science. 1983. PMID: 6190229
Electroendosmosis, on the other hand, proceeds in the cathodal direction. These opposing fluxes separate the hemoglobins in the order of their affinity for agaropectin. An agaropectin binding site was identified on hemoglobin by computer-assisted modeling, and the r …
Electroendosmosis, on the other hand, proceeds in the cathodal direction. These opposing fluxes separate the hemoglobins in the order …
Paper-based microchip electrophoresis for point-of-care hemoglobin testing.
Hasan MN , Fraiwan A , An R , Alapan Y , Ung R , Akkus A , Xu JZ , Rezac AJ , Kocmich NJ , Creary MS , Oginni T , Olanipekun GM , Hassan-Hanga F , Jibir BW , Gambo S , Verma AK , Bharti PK , Riolueang S , Ngimhung T , Suksangpleng T , Thota P , Werner G , Shanmugam R , Das A , Viprakasit V , Piccone CM , Little JA , Obaro SK , Gurkan UA . Hasan MN , et al. Analyst. 2020 Apr 7;145(7):2525-2542. doi: 10.1039/c9an02250c. Epub 2020 Mar 3. Analyst. 2020. PMID: 32123889 Free PMC article.
Nearly 7% of the world's population live with a hemoglobin variant. Hemoglobins S, C, and E are the most common and significant hemoglobin variants worldwide. Sickle cell disease, caused by hemoglobin S, is highly prevalent in sub-Saharan Africa …
Nearly 7% of the world's population live with a hemoglobin variant. Hemoglobins S, C, and E are the most common and significan …
Composition of the hemoglobin S polymer.
Bookchin RM, Balazs T, Lew VL. Bookchin RM, et al. Am J Hematol. 1993 Jan;42(1):118-21. doi: 10.1002/ajh.2830420123. Am J Hematol. 1993. PMID: 8416285 Review. No abstract available.
The unstable haemoglobins.
Williamson D. Williamson D. Blood Rev. 1993 Sep;7(3):146-63. doi: 10.1016/0268-960x(93)90002-l. Blood Rev. 1993. PMID: 8241830 Review.
The unstable haemoglobin haemolytic anaemias result from the presence in the red cell of a structurally abnormal haemoglobin variant. There are many mutations producing unstable haemoglobins; most are single amino acid replacements that affect a few key areas …
The unstable haemoglobin haemolytic anaemias result from the presence in the red cell of a structurally abnormal haemoglobin v …
193,920 results
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